ID EGFR_HUMAN STANDARD; PRT; 1210 AA. AC P00533; O00688; O00732; P06268; Q14225; Q92795; Q9BZS2; Q9GZX1; AC Q9H2C9; Q9H3C9; Q9UMD7; Q9UMD8; Q9UMG5; DT 21-JUL-1986 (Rel. 01, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 01-OCT-2004 (Rel. 45, Last annotation update) DE Epidermal growth factor receptor precursor (EC 2.7.1.112) (Receptor DE protein-tyrosine kinase ErbB-1). GN Name=EGFR; Synonyms=ERBB1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. (ISOFORM 1). RX MEDLINE=84219729; PubMed=6328312; RA Ullrich A., Coussens L., Hayflick J.S., Dull T.J., Gray A., Tam A.W., RA Lee J., Yarden Y., Libermann T.A., Schlessinger J., Downward J., RA Mayes E.L.V., Whittle N., Waterfield M.D., Seeburg P.H.; RT "Human epidermal growth factor receptor cDNA sequence and aberrant RT expression of the amplified gene in A431 epidermoid carcinoma cells."; RL Nature 309:418-425(1984). RN [2] RP SEQUENCE FROM N.A. (ISOFORM 2). RC TISSUE=Placenta; RX MEDLINE=95382957; PubMed=7654368; RA Ilekis J.V., Stark B.C., Scoccia B.; RT "Possible role of variant RNA transcripts in the regulation of RT epidermal growth factor receptor expression in human placenta."; RL Mol. Reprod. Dev. 41:149-156(1995). RN [3] RP SEQUENCE FROM N.A. (ISOFORM 2). RC TISSUE=Placenta; RX MEDLINE=97078686; PubMed=8918811; RA Reiter J.L., Maihle N.J.; RT "A 1.8 kb alternative transcript from the human epidermal growth RT factor receptor gene encodes a truncated form of the receptor."; RL Nucleic Acids Res. 24:4050-4056(1996). RN [4] RP SEQUENCE FROM N.A. (ISOFORM 2). RC TISSUE=Placenta; RX MEDLINE=97256547; PubMed=9103388; RA Ilekis J.V., Gariti J., Niederberger C., Scoccia B.; RT "Expression of a truncated epidermal growth factor receptor-like RT protein (TEGFR) in ovarian cancer."; RL Gynecol. Oncol. 65:36-41(1997). RN [5] RP SEQUENCE FROM N.A. (ISOFORMS 3 AND 4). RC TISSUE=Placenta; RX MEDLINE=21100872; PubMed=11161793; DOI=10.1006/geno.2000.6341; RA Reiter J.L., Threadgill D.W., Eley G.D., Strunk K.E., Danielsen A.J., RA Schehl Sinclair C., Pearsall R.S., Green P.J., Yee D., Lampland A.L., RA Balasubramaniam S., Crossley T.D., Magnuson T.R., James C.D., RA Maihle N.J.; RT "Comparative genomic sequence analysis and isolation of human and RT mouse alternative EGFR transcripts encoding truncated receptor RT isoforms."; RL Genomics 71:1-20(2001). RN [6] RP SEQUENCE FROM N.A. (ISOFORM 1), AND VARIANTS GLN-98; ARG-266; LYS-521; RP ILE-674; GLY-962 AND PRO-988. RA Livingston R.J., Rieder M.J., Chung M.-W., Ritchie T.K., Olson A.N., RA Nguyen C.P., Nguyen D.A., Poel C.L., Robertson P.D., Schackwitz W.S., RA Sherwood J.K., Sherwood A.M., Leithauser B.J., Nickerson D.A.; RT "NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department RT of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu)."; RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases. RN [7] RP SEQUENCE OF 575-687 FROM N.A. RA Reiter J.L., Threadgill D.W., Danielsen A.J., Schehl C.M., RA Lampland A.L., Balasubramaniam S., Crossley T.O., Magnuson T.R., RA Maihle N.J.; RT "Human and mouse alternative EGFR transcripts encoding only the RT extracellular domain of the receptor."; RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases. RN [8] RP SEQUENCE OF 713-924 FROM N.A. RX MEDLINE=84196372; PubMed=6326261; RA Lin C.R., Chen W.S., Kruiger W., Stolarsky L.S., Weber W., Evans R.M., RA Verma I.M., Gill G.N., Rosenfeld M.G.; RT "Expression cloning of human EGF receptor complementary DNA: gene RT amplification and three related messenger RNA products in A431 RT cells."; RL Science 224:843-848(1984). RN [9] RP SEQUENCE OF 150-962 FROM N.A. RX MEDLINE=84245835; PubMed=6330563; RA Xu Y.H., Ishii S., Clark A.J.L., Sullivan M., Wilson R.K., Ma D.P., RA Roe B.A., Merlino G.T., Pastan I.; RT "Human epidermal growth factor receptor cDNA is homologous to a RT variety of RNAs overproduced in A431 carcinoma cells."; RL Nature 309:806-810(1984). RN [10] RP SEQUENCE OF 1028-1210 FROM N.A. RX MEDLINE=85046483; PubMed=6093780; RA Simmen F.A., Gope M.L., Schulz T.Z., Wright D.A., Carpenter G., RA O'Malley B.W.; RT "Isolation of an evolutionarily conserved epidermal growth factor RT receptor cDNA from human A431 carcinoma cells."; RL Biochem. Biophys. Res. Commun. 124:125-132(1984). RN [11] RP SEQUENCE OF 1-29 FROM N.A. RX MEDLINE=88217333; PubMed=3329716; RA Haley J.D., Whittle N., Bennett P., Kinchington D., Ullrich A., RA Waterfield M.D.; RT "The human EGF receptor gene: structure of the 110 kb locus and RT identification of sequences regulating its transcription."; RL Oncogene Res. 1:375-396(1987). RN [12] RP SEQUENCE OF 1-29 FROM N.A. RX MEDLINE=91107677; PubMed=1988448; RA Haley J.D., Waterfield M.D.; RT "Contributory effects of de novo transcription and premature RT transcript termination in the regulation of human epidermal growth RT factor receptor proto-oncogene RNA synthesis."; RL J. Biol. Chem. 266:1746-1753(1991). RN [13] RP SEQUENCE OF 1-29 FROM N.A. RX MEDLINE=85270438; PubMed=2991899; RA Ishii S., Xu Y.H., Stratton R.H., Roe B.A., Merlino G.T., Pastan I.; RT "Characterization and sequence of the promoter region of the human RT epidermal growth factor receptor gene."; RL Proc. Natl. Acad. Sci. U.S.A. 82:4920-4924(1985). RN [14] RP SEQUENCE OF 540. RA Kohda D.; RL Submitted (SEP-1997) to Swiss-Prot. RN [15] RP SEQUENCE OF 687-705; 986-998; 1000-1023; 1026-1030 AND 1068-1077, AND RP PHOSPHORYLATION SITES THR-693; SER-695; SER-1070 AND SER-1071. RX PubMed=3138233; RA Heisermann G.J., Gill G.N.; RT "Epidermal growth factor receptor threonine and serine residues RT phosphorylated in vivo."; RL J. Biol. Chem. 263:13152-13158(1988). RN [16] RP SEQUENCE OF 25-39. RA Zhang Z., Henzel W.; RT "Signal peptide prediction based on analysis of experimentally RT verified cleavage sites."; RL Submitted (JUN-2004) to Swiss-Prot. RN [17] RP RECEPTOR ACTIVITY. RX MEDLINE=84191554; PubMed=6325948; RA Mroczkowski B., Mosig G., Cohen S.; RT "ATP-stimulated interaction between epidermal growth factor receptor RT and supercoiled DNA."; RL Nature 309:270-273(1984). RN [18] RP PHOSPHORYLATION. RX MEDLINE=89278137; PubMed=2543678; RA Margolis B.L., Lax I., Kris R., Dombalagian M., Honegger A.M., RA Howk R., Givol D., Ullrich A., Schlessinger J.; RT "All autophosphorylation sites of epidermal growth factor (EGF) RT receptor and HER2/neu are located in their carboxyl-terminal tails. RT Identification of a novel site in EGF receptor."; RL J. Biol. Chem. 264:10667-10671(1989). RN [19] RP CARBOHYDRATE-LINKAGE SITES ASN-128; ASN-175; ASN-413; ASN-444 AND RP ASN-528. RX MEDLINE=96398132; PubMed=8962717; RA Smith K.D., Davies M.J., Bailey D., Renouf D.V., Hounsell E.F.; RT "Analysis of the glycosylation patterns of the extracellular domain of RT the epidermal growth factor receptor expressed in Chinese hamster RT ovary fibroblasts."; RL Growth Factors 13:121-132(1996). RN [20] RP CARBOHYDRATE-LINKAGE SITES ASN-56; ASN-352; ASN-361; ASN-568 AND RP ASN-603. RX MEDLINE=20198209; PubMed=10731668; RA Sato C., Kim J.-H., Abe Y., Saito K., Yokoyama S., Kohda D.; RT "Characterization of the N-oligosaccharides attached to the atypical RT Asn-X-Cys sequence of recombinant human epidermal growth factor RT receptor."; RL J. Biochem. 127:65-72(2000). RN [21] RP PARTIAL SEQUENCE, AND DISULFIDE BONDS. RX MEDLINE=98225196; PubMed=9556602; RA Abe Y., Odaka M., Inagaki F., Lax I., Schlessinger J., Kohda D.; RT "Disulfide bond structure of human epidermal growth factor receptor."; RL J. Biol. Chem. 273:11150-11157(1998). RN [22] RP REVIEW. RX MEDLINE=87297456; PubMed=3039909; RA Carpenter G.; RT "Receptors for epidermal growth factor and other polypeptide RT mitogens."; RL Annu. Rev. Biochem. 56:881-914(1987). RN [23] RP INTERACTION WITH CBL. RX MEDLINE=95386455; PubMed=7657591; RA Galisteo M.L., Dikic I., Batzer A.G., Langdon W.Y., Schlessinger J.; RT "Tyrosine phosphorylation of the c-cbl proto-oncogene protein product RT and association with epidermal growth factor (EGF) receptor upon EGF RT stimulation."; RL J. Biol. Chem. 270:20242-20245(1995). RN [24] RP INTERACTION WITH RIPK1. RX MEDLINE=21153697; PubMed=11116146; DOI=10.1074/jbc.M008458200; RA Habib A.A., Chatterjee S., Park S.-K., Ratan R.R., Lefebvre S., RA Vartanian T.; RT "The epidermal growth factor receptor engages receptor interacting RT protein and nuclear factor-kappa B (NF-kappa B)-inducing kinase to RT activate NF-kappa B. Identification of a novel receptor-tyrosine RT kinase signalosome."; RL J. Biol. Chem. 276:8865-8874(2001). RN [25] RP VARIANTS LUNG CANCER SER-719 AND ARG-858. RX PubMed=15118125; DOI=10.1126/science.1099314; RA Paez J.G., Janne P.A., Lee J.C., Tracy S., Greulich H., Gabriel S., RA Herman P., Kaye F.J., Lindeman N., Boggon T.J., Naoki K., Sasaki H., RA Fujii Y., Eck M.J., Sellers W.R., Johnson B.E., Meyerson M.; RT "EGFR mutations in lung cancer: correlation with clinical response to RT gefitinib therapy."; RL Science 304:1497-1500(2004). CC -!- FUNCTION: Receptor for EGF, but also for other members of the EGF CC family, as TGF-alpha, amphiregulin, betacellulin, heparin-binding CC EGF-like growth factor, GP30 and vaccinia virus growth factor. Is CC involved in the control of cell growth and differentiation. CC -!- FUNCTION: Isoform 2/truncated isoform may act as an antagonist. CC -!- CATALYTIC ACTIVITY: ATP + a protein tyrosine = ADP + protein CC tyrosine phosphate. CC -!- SUBUNIT: Binds RIPK1. CBL interacts with the autophosphorylated C- CC terminal tail of the EGF receptor. CC -!- SUBCELLULAR LOCATION: Type I membrane protein. Isoform 2 is CC secreted. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; Synonyms=p170; CC IsoId=P00533-1; Sequence=Displayed; CC Name=2; Synonyms=p60, Truncated, TEGFR; CC IsoId=P00533-2; Sequence=VSP_002887, VSP_002888; CC Name=3; Synonyms=p110; CC IsoId=P00533-3; Sequence=VSP_002889, VSP_002890; CC Name=4; CC IsoId=P00533-4; Sequence=VSP_002891, VSP_002892; CC -!- TISSUE SPECIFICITY: Expressed in placenta. Isoform 2 is also CC expressed in ovarian cancers. CC -!- PTM: Phosphorylation of Ser-695 is partial and occurs only if Thr- CC 693 is phosphorylated. CC -!- DISEASE: Defects in EGFR are associated with lung cancer. CC -!- MISCELLANEOUS: Binding of EGF to the receptor leads to CC dimerization, internalization of the EGF-receptor complex, CC induction of the tyrosine kinase activity, stimulation of cell DNA CC synthesis, and cell proliferation. CC -!- SIMILARITY: Belongs to the EGF receptor family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X00588; CAA25240.1; -. DR EMBL; U95089; AAB53063.1; -. DR EMBL; U48722; AAC50802.1; -. DR EMBL; U48723; AAC50804.1; -. DR EMBL; U48724; AAC50796.1; -. DR EMBL; U48725; AAC50797.1; -. DR EMBL; U48726; AAC50798.1; -. DR EMBL; U48727; AAC50799.1; -. DR EMBL; U48728; AAC50800.1; -. DR EMBL; U48729; AAC50801.1; -. DR EMBL; AF288738; AAG35786.1; -. DR EMBL; AF288738; AAG35787.1; -. DR EMBL; AF288738; AAG35788.1; -. DR EMBL; AF288738; AAG35789.1; -. DR EMBL; AF288738; AAG35790.1; -. DR EMBL; AY588246; AAS83109.1; -. DR EMBL; AF277897; AAK01080.1; -. DR EMBL; AF125253; AAG43240.1; -. DR EMBL; AF125539; AAG43243.1; -. DR EMBL; AF125538; AAG43243.1; JOINED. DR EMBL; X06370; CAA29668.1; -. DR EMBL; X00663; CAA25282.1; -. DR EMBL; M38425; AAA63171.1; -. DR EMBL; M11234; AAA52370.1; -. DR PIR; A00641; GQHUE. DR PDB; 1DNQ; 12-APR-00. DR PDB; 1DNR; 12-APR-00. DR PDB; 1IVO; 16-OCT-02. DR PDB; 1M14; 25-FEB-03. DR PDB; 1M17; 25-FEB-03. DR IntAct; P00533; -. DR GlycoSuiteDB; P00533; -. DR SWISS-2DPAGE; P00533; HUMAN. DR Genew; HGNC:3236; EGFR. DR MIM; 131550; -. DR GO; GO:0005768; C:endosome; TAS. DR GO; GO:0005886; C:plasma membrane; TAS. DR GO; GO:0008283; P:cell proliferation; TAS. DR GO; GO:0007173; P:epidermal growth factor receptor signaling ...; TAS. DR InterPro; IPR001450; 4Fe4S_ferredoxin. DR InterPro; IPR000494; EGFR_L. DR InterPro; IPR006211; Furin-like. DR InterPro; IPR009030; Grow_fac_recept. DR InterPro; IPR011009; Kinase_like. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR001245; Tyr_pkinase. DR InterPro; IPR008266; Tyr_pkinase_AS. DR Pfam; PF00757; Furin-like; 1. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF01030; Recep_L_domain; 2. DR PRINTS; PR00353; 4FE4SFRDOXIN. DR PRINTS; PR00109; TYRKINASE. DR ProDom; PD000001; Prot_kinase; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. KW 3D-structure; Alternative splicing; Anti-oncogene; ATP-binding; KW Direct protein sequencing; Disease mutation; Glycoprotein; KW Phosphorylation; Polymorphism; Receptor; Repeat; Signal; Transferase; KW Transmembrane; Tyrosine-protein kinase. FT SIGNAL 1 24 FT CHAIN 25 1210 Epidermal growth factor receptor. FT DOMAIN 25 645 Extracellular (Potential). FT TRANSMEM 646 668 Potential. FT DOMAIN 669 1210 Cytoplasmic (Potential). FT REPEAT 75 300 Approximate. FT REPEAT 390 600 Approximate. FT DOMAIN 1025 1071 Ser-rich. FT DOMAIN 712 979 Protein kinase. FT NP_BIND 718 726 ATP (By similarity). FT BINDING 745 745 ATP (By similarity). FT ACT_SITE 837 837 By similarity. FT DISULFID 190 199 FT DISULFID 194 207 FT DISULFID 215 223 FT DISULFID 219 231 FT DISULFID 232 240 FT DISULFID 236 248 FT DISULFID 251 260 FT DISULFID 264 291 FT DISULFID 295 307 FT DISULFID 311 326 FT DISULFID 329 333 FT DISULFID 506 515 FT DISULFID 510 523 FT DISULFID 526 535 FT DISULFID 539 555 FT DISULFID 558 571 FT DISULFID 562 579 FT DISULFID 582 591 FT DISULFID 595 617 FT DISULFID 620 628 FT DISULFID 624 636 FT MOD_RES 678 678 Phosphothreonine (by PKC). FT MOD_RES 693 693 Phosphothreonine. FT MOD_RES 695 695 Phosphoserine (partial). FT MOD_RES 1070 1070 Phosphoserine. FT MOD_RES 1071 1071 Phosphoserine. FT MOD_RES 1092 1092 Phosphotyrosine (by autocatalysis) FT (partial). FT MOD_RES 1110 1110 Phosphotyrosine (by autocatalysis) FT (partial). FT MOD_RES 1172 1172 Phosphotyrosine (by autocatalysis) FT (partial). FT MOD_RES 1197 1197 Phosphotyrosine (by autocatalysis). FT CARBOHYD 56 56 N-linked (GlcNAc...) (complex). FT /FTId=CAR_000227. FT CARBOHYD 128 128 N-linked (GlcNAc...). FT CARBOHYD 175 175 N-linked (GlcNAc...). FT CARBOHYD 352 352 N-linked (GlcNAc...). FT CARBOHYD 361 361 N-linked (GlcNAc...). FT CARBOHYD 413 413 N-linked (GlcNAc...). FT CARBOHYD 444 444 N-linked (GlcNAc...). FT CARBOHYD 528 528 N-linked (GlcNAc...). FT CARBOHYD 568 568 N-linked (GlcNAc...). FT CARBOHYD 603 603 N-linked (GlcNAc...). FT VARSPLIC 404 405 FL -> LS (in isoform 2). FT /FTId=VSP_002887. FT VARSPLIC 406 1210 Missing (in isoform 2). FT /FTId=VSP_002888. FT VARSPLIC 628 705 CTGPGLEGCPTNGPKIPSIATGMVGALLLLLVVALGIGLFM FT RRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQALLR -> FT PGNESLKAMLFCLFKLSSCNQSNDGSVSHQSGSPAAQESCL FT GWIPSLLPSEFQLGWGGCSHLHAWPSASVIITASSCH (in FT isoform 3). FT /FTId=VSP_002889. FT VARSPLIC 706 1210 Missing (in isoform 3). FT /FTId=VSP_002890. FT VARSPLIC 628 628 C -> S (in isoform 4). FT /FTId=VSP_002891. FT VARSPLIC 629 1210 Missing (in isoform 4). FT /FTId=VSP_002892. FT VARIANT 98 98 R -> Q. FT /FTId=VAR_019293. FT VARIANT 266 266 P -> R. FT /FTId=VAR_019294. FT VARIANT 521 521 R -> K. FT /FTId=VAR_019295. FT VARIANT 674 674 V -> I. FT /FTId=VAR_019296. FT VARIANT 719 719 G -> S (in lung cancer; somatic FT mutation). FT /FTId=VAR_019297. FT VARIANT 858 858 L -> R (in lung cancer; somatic FT mutation). FT /FTId=VAR_019298. FT VARIANT 962 962 R -> G. FT /FTId=VAR_019299. FT VARIANT 988 988 H -> P. FT /FTId=VAR_019300. FT CONFLICT 540 540 N -> K (in Ref. 1). FT STRAND 30 31 FT TURN 37 38 FT STRAND 40 41 FT TURN 44 45 FT HELIX 46 55 FT TURN 56 57 FT STRAND 60 61 FT STRAND 65 68 FT TURN 72 73 FT HELIX 77 81 FT STRAND 84 85 FT STRAND 89 92 FT STRAND 98 98 FT TURN 101 102 FT STRAND 106 107 FT STRAND 119 122 FT TURN 127 129 FT STRAND 134 134 FT TURN 138 139 FT STRAND 142 143 FT STRAND 148 151 FT TURN 154 155 FT HELIX 159 161 FT TURN 164 167 FT STRAND 168 168 FT HELIX 170 173 FT TURN 174 175 FT STRAND 178 178 FT TURN 192 193 FT TURN 195 196 FT STRAND 199 199 FT TURN 204 205 FT STRAND 207 207 FT STRAND 223 223 FT TURN 228 229 FT STRAND 231 231 FT TURN 234 235 FT STRAND 236 240 FT STRAND 248 251 FT STRAND 254 256 FT TURN 257 258 FT STRAND 259 261 FT STRAND 268 271 FT TURN 272 275 FT STRAND 276 279 FT STRAND 285 287 FT TURN 288 289 FT STRAND 290 292 FT TURN 297 298 FT STRAND 300 301 FT TURN 303 304 FT STRAND 306 308 FT TURN 313 314 FT STRAND 315 315 FT STRAND 324 324 FT STRAND 328 328 FT STRAND 337 337 FT STRAND 340 340 FT TURN 341 341 FT HELIX 343 345 FT TURN 354 355 FT HELIX 357 359 FT STRAND 364 365 FT STRAND 368 371 FT HELIX 373 377 FT STRAND 379 379 FT TURN 380 383 FT STRAND 384 384 FT HELIX 389 397 FT STRAND 400 401 FT STRAND 405 407 FT STRAND 416 416 FT TURN 419 420 FT STRAND 425 426 FT STRAND 432 432 FT TURN 433 435 FT STRAND 436 441 FT STRAND 447 447 FT STRAND 455 456 FT STRAND 460 464 FT TURN 467 468 FT HELIX 472 474 FT HELIX 477 479 FT TURN 480 480 FT TURN 484 485 FT STRAND 488 489 FT HELIX 496 499 FT TURN 500 502 FT STRAND 507 507 FT TURN 508 509 FT STRAND 510 510 FT TURN 512 513 FT STRAND 515 515 FT HELIX 520 522 FT STRAND 523 523 FT TURN 528 529 FT STRAND 706 706 FT HELIX 709 711 FT STRAND 712 719 FT TURN 721 723 FT STRAND 724 731 FT STRAND 740 747 FT HELIX 753 767 FT TURN 768 768 FT TURN 772 773 FT STRAND 774 774 FT STRAND 777 782 FT STRAND 786 791 FT TURN 794 795 FT STRAND 797 797 FT HELIX 798 805 FT HELIX 806 808 FT HELIX 811 830 FT TURN 831 832 FT STRAND 833 834 FT HELIX 840 842 FT STRAND 843 847 FT TURN 848 849 FT STRAND 850 853 FT TURN 857 858 FT STRAND 860 861 FT STRAND 869 870 FT HELIX 878 880 FT HELIX 883 888 FT STRAND 890 891 FT HELIX 893 908 FT TURN 909 910 FT TURN 914 915 FT HELIX 920 929 FT TURN 930 930 FT TURN 937 938 FT STRAND 939 939 FT HELIX 941 950 FT TURN 951 951 FT HELIX 955 957 FT HELIX 961 972 FT TURN 973 973 FT HELIX 975 977 FT TURN 978 978 FT STRAND 979 979 FT HELIX 1013 1015 SQ SEQUENCE 1210 AA; 134277 MW; D8A2A50B4EFB6ED2 CRC64; MRPSGTAGAA LLALLAALCP ASRALEEKKV CQGTSNKLTQ LGTFEDHFLS LQRMFNNCEV VLGNLEITYV QRNYDLSFLK TIQEVAGYVL IALNTVERIP LENLQIIRGN MYYENSYALA VLSNYDANKT GLKELPMRNL QEILHGAVRF SNNPALCNVE SIQWRDIVSS DFLSNMSMDF QNHLGSCQKC DPSCPNGSCW GAGEENCQKL TKIICAQQCS GRCRGKSPSD CCHNQCAAGC TGPRESDCLV CRKFRDEATC KDTCPPLMLY NPTTYQMDVN PEGKYSFGAT CVKKCPRNYV VTDHGSCVRA CGADSYEMEE DGVRKCKKCE GPCRKVCNGI GIGEFKDSLS INATNIKHFK NCTSISGDLH ILPVAFRGDS FTHTPPLDPQ ELDILKTVKE ITGFLLIQAW PENRTDLHAF ENLEIIRGRT KQHGQFSLAV VSLNITSLGL RSLKEISDGD VIISGNKNLC YANTINWKKL FGTSGQKTKI ISNRGENSCK ATGQVCHALC SPEGCWGPEP RDCVSCRNVS RGRECVDKCN LLEGEPREFV ENSECIQCHP ECLPQAMNIT CTGRGPDNCI QCAHYIDGPH CVKTCPAGVM GENNTLVWKY ADAGHVCHLC HPNCTYGCTG PGLEGCPTNG PKIPSIATGM VGALLLLLVV ALGIGLFMRR RHIVRKRTLR RLLQERELVE PLTPSGEAPN QALLRILKET EFKKIKVLGS GAFGTVYKGL WIPEGEKVKI PVAIKELREA TSPKANKEIL DEAYVMASVD NPHVCRLLGI CLTSTVQLIT QLMPFGCLLD YVREHKDNIG SQYLLNWCVQ IAKGMNYLED RRLVHRDLAA RNVLVKTPQH VKITDFGLAK LLGAEEKEYH AEGGKVPIKW MALESILHRI YTHQSDVWSY GVTVWELMTF GSKPYDGIPA SEISSILEKG ERLPQPPICT IDVYMIMVKC WMIDADSRPK FRELIIEFSK MARDPQRYLV IQGDERMHLP SPTDSNFYRA LMDEEDMDDV VDADEYLIPQ QGFFSSPSTS RTPLLSSLSA TSNNSTVACI DRNGLQSCPI KEDSFLQRYS SDPTGALTED SIDDTFLPVP EYINQSVPKR PAGSVQNPVY HNQPLNPAPS RDPHYQDPHS TAVGNPEYLN TVQPTCVNST FDSPAHWAQK GSHQISLDNP DYQQDFFPKE AKPNGIFKGS TAENAEYLRV APQSSEFIGA //